Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
The stimulation of the phosphoinositide phospholipase C ( PI / PLC ) activity can be blocked by incubation of GH 3 membranes with polyclonal antibodies directed against a peptide derived from the C terminal region of G alpha q and G alpha 11 . ^^^ |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
PLC beta 2 mRNA levels were similarly reduced compared with GPIIb and Galphaq mRNA levels . ^^^ |
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Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
Role of Galphaq and phospholipase C beta 2 in human platelets activation by thrombin receptors PAR 1 and PAR 4 : studies in human platelets deficient in Galphaq and phospholipase C beta 2 . ^^^ We assessed cytoplasmic Ca2+ mobilization in response to activation with thrombin and PAR 1 ( SFLLRN ) and PAR 4 ( GYPGKF ) peptides in two patients whose platelets were deficient in two major signalling proteins , Galphaq or phospholipase ( PLC ) beta 2 . ^^^ At higher concentrations , it was decreased in PLC beta 2 deficient platelets ; the sustained Ca2+ elevation observed in normal and Galphaq deficient platelets was reduced in PLC beta 2 deficient platelets . ^^^ These studies provide evidence that , in human platelets , both Galphaq and PLC beta 2 play a major role in responses to PAR 1 and PAR 4 activation , and that PLC beta 2 is required for the sustained Ca2+ rise upon thrombin activation . . ^^^ |
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Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
Relative to other PLC beta isoenzymes , PLC betaX was less sensitive to stimulation by Galphaq than PLC beta 1 but similar to PLC beta 2 and PLC betaT . ^^^ |
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Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
The affinity of Galphaq ( GTPgammaS ) is similar for PLC beta 1 and beta 3 and 10 fold stronger for PLC beta 2 , which corresponds to the reported relationship between the concentration of Galphaq ( GTPgammaS ) and PLC beta activation on lipid bilayers . ^^^ We also tested the possibility that both Galphaq and Gbetagamma can simultaneously bind PLC beta 2 . ^^^ |
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Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
These results indicate that the C 2 domains of PLC beta 1 and PLC beta 2 provide a surface to which Galphaq subunits can dock , leading to activation of the native protein . . ^^^ |
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Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q00722 and P50148 |
Pubmed |
SVM Score :0.0 |
NA |
|